CBLC

CBL proteins, such as CBLC, are phosphorylated upon activation of a variety of receptors that signal via protein tyrosine kinases. Through interactions with proteins containing SRC (MIM 190090) homology-2 (SH2) and SH3 domains, CBL proteins modulate downstream cell signaling (Keane et al., 1999 [PubMed 10362357]).[supplied by OMIM

Cas-Br-M (murine) ecotropic retroviral transforming sequence c

Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Functionally coupled with the E2 ubiquitin-protein ligases UB2D1, UB2D2 and UB2D3. Regulator of EGFR mediated signal transduction; upon EGF activation, ubiquitinates EGFR. Isoform 1, but not isoform 2, inhibits EGF stimulated MAPK1 activation. Promotes ubiquitination of SRC phosphorylated at 'Tyr-419'. In collaboration with CD2AP may act as regulatory checkpoint for Ret signaling by modulating the rate of RET degradation after ligand activation; CD2AP converts it from an inhibitor to a promoter of RET degradation; the function limits the potency of GDNF on neuronal survival.

Cell surface receptor signaling pathway Source: InterPro
Negative regulation of epidermal growth factor-activated receptor activity Source: BHF-UCL
Negative regulation of epidermal growth factor receptor signaling pathway Source: BHF-UCL
Negative regulation of MAP kinase activity Source: BHF-UCL
Protein ubiquitination Source: BHF-UCL
Signal transduction Source: GO_Central
Ubiquitin-dependent protein catabolic process Source: BHF-UCL

Plasma membrane; Membrane raft

Phosphorylated on multiple tyrosine residues by SRC. Isoform 1, but not isoform 2, is phosphorylated on tyrosines by EGFR.
Autoubiquitinated when phosphorylated at Tyr-341, enhanced by SRC; suggesting proteasomal degradation.